CQSS_VIBCH
ID CQSS_VIBCH Reviewed; 686 AA.
AC Q9KM66;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=CAI-1 autoinducer sensor kinase/phosphatase CqsS;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
DE AltName: Full=Cholerae quorum-sensing sensor;
GN Name=cqsS; OrderedLocusNames=VC_A0522;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION AS THE CAI-1 SENSOR.
RX PubMed=12176318; DOI=10.1016/s0092-8674(02)00829-2;
RA Miller M.B., Skorupski K., Lenz D.H., Taylor R.K., Bassler B.L.;
RT "Parallel quorum sensing systems converge to regulate virulence in Vibrio
RT cholerae.";
RL Cell 110:303-314(2002).
RN [3]
RP IDENTIFICATION OF CAI-1.
RX PubMed=18004304; DOI=10.1038/nature06284;
RA Higgins D.A., Pomianek M.E., Kraml C.M., Taylor R.K., Semmelhack M.F.,
RA Bassler B.L.;
RT "The major Vibrio cholerae autoinducer and its role in virulence factor
RT production.";
RL Nature 450:883-886(2007).
CC -!- FUNCTION: Senses the quorum-sensing autoinducer CAI-1 ((S)-3-
CC hydroxytridecan-4-one) which probably functions as an intragenus
CC signal. The sensory signal is then relayed to LuxU and LuxO.
CC {ECO:0000269|PubMed:12176318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AE003853; AAF96425.1; -; Genomic_DNA.
DR PIR; G82448; G82448.
DR RefSeq; NP_232913.1; NC_002506.1.
DR AlphaFoldDB; Q9KM66; -.
DR SMR; Q9KM66; -.
DR STRING; 243277.VC_A0522; -.
DR BindingDB; Q9KM66; -.
DR ChEMBL; CHEMBL1921662; -.
DR DNASU; 2612235; -.
DR EnsemblBacteria; AAF96425; AAF96425; VC_A0522.
DR KEGG; vch:VC_A0522; -.
DR PATRIC; fig|243277.26.peg.3148; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_104_18_6; -.
DR OMA; MSFMSAI; -.
DR BioCyc; VCHO:VCA0522-MON; -.
DR PRO; PR:Q9KM66; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hydrolase; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..686
FT /note="CAI-1 autoinducer sensor kinase/phosphatase CqsS"
FT /id="PRO_0000316891"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 191..416
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 569..686
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 194
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 618
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 686 AA; 78382 MW; 0662BF71AF3B9562 CRC64;
MIVSMDVIKR VYQYAEPNLS LVGWMGMLGF PAYYFIWEYW FPQSYENLGL RCAAAVLFGG
LVFRDSMPKK WQRYMPGYFL FTIGFCLPFF FAFMMLMNDW STIWAMSFMA SIFLHILLVH
DTRVMALQAL FSVLVAYLAV YGLTDFHPTT LIEWQYIPIF LFTYVFGNLC FFRNQISHET
KVSIAKTFGA GIAHEMRNPL SALKTSIDVV RTMIPKPQTA AHTDYSLDAQ ELDLLHQILN
EADDVIYSGN NAIDLLLTSI DENRVSPASF KKHSVVDVIE KAVKTFPYKN AADQHSVELE
VHQPFDFFGS DTLLTYALFN LLKNAFYYQK EHFSVCISIE QTSEHNLIRV RDNGVGIAPE
MLEDIFRDFY TFGKNGSYGL GLPFCRKVMS AFGGTIRCAS QQGQWTEFVL SFPRYDSDTV
NEIKTELLKT KSLIYIGSNQ AIVRELNQLA VEDEFGFTAI SAQQAVRRQD YEFEFDLILL
DLDDATAQGE LLPKLEGTLS FAEGCIGYVY DPGKTYAVNI NRYLRIQPIS IHSILRKPRK
IIERLLFEQE SLSMNRNVIP LQKSRHERRI LVVDDNQSIR TFTAILLEQQ GYEVVQANDG
SEVLKHMESQ NIDLVLMDIE MPNVGGLEAT RLIRNSEHEY KNIPIIGYTG DNSPKTLALV
QTSGMNDFIV KPADRDVLLN KVAAWV
